Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4MRR

Structure of a bacterial Atm1-family ABC transporter

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0046689biological_processresponse to mercury ion
A0055085biological_processtransmembrane transport
A0140359molecular_functionABC-type transporter activity
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0046689biological_processresponse to mercury ion
B0055085biological_processtransmembrane transport
B0140359molecular_functionABC-type transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE LDA A 701
ChainResidue
ATHR113
ALEU116
AGLY147
ATHR148
AASP331
AGLU334
AMSE335

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LDA A 702
ChainResidue
BILE144
BLDA702
AASP217
ATYR247

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 704
ChainResidue
AARG114
AHIS115
BARG252

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 705
ChainResidue
ASER396
AGLY399
ALYS400
ASER401

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 706
ChainResidue
AARG206
AARG210
AMSE320
AARG323

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE LDA B 701
ChainResidue
AVAL120
ALEU124
ATHR148
BASP217
BTYR247

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LDA B 702
ChainResidue
ALDA702
BTHR113
BGLY147
BASP331
BGLU334
BMSE335

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 704
ChainResidue
BSER396
BGLY399
BLYS400
BSER401

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 705
ChainResidue
AARG252
BARG114
BHIS115

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 706
ChainResidue
BARG206
BARG210
BMSE320
BARG323

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGEKQRVAIARTL
ChainResidueDetails
ALEU498-LEU512

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues866
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24604198
ChainResidueDetails
AMSE1-ARG38
AGLU106-MSE154
ATHR203-GLY266
AARG323-GLU608
BMSE1-ARG38
BGLU106-MSE154
BTHR203-GLY266
BARG323-GLU608

site_idSWS_FT_FI2
Number of Residues254
DetailsTRANSMEM: Helical
ChainResidueDetails
AVAL39-TYR60
BPHE180-ILE202
BLEU267-ALA285
BLEU301-TYR322
APHE83-PHE105
ALEU155-LEU178
APHE180-ILE202
ALEU267-ALA285
ALEU301-TYR322
BVAL39-TYR60
BPHE83-PHE105
BLEU155-LEU178

site_idSWS_FT_FI3
Number of Residues72
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:24604198
ChainResidueDetails
ALYS61-ALA82
AASN179
ATRP286-ASP300
BLYS61-ALA82
BASN179
BTRP286-ASP300

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P40416
ChainResidueDetails
AARG206
BARG206

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:24604198, ECO:0007744|PDB:4MRP
ChainResidueDetails
AASN269
AASP316
BASN269
BASP316

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9NP58
ChainResidueDetails
ATYR370
BTYR370

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY394
BGLY394

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon